• The Korean Journal of Pesticide Science
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• v.17 no.1
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• pp.1-5
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• 2013

This study was conducted to the amount of pesticide residue in 21 different kinds of 100 commercial flowering teas. Multi-residue analyses of 203 pesticides was performed using the GC-ECD, GC-NPD, GC-MSD, and LC-MS/MS. Pesticide residues were detected in 4 samples (4%) of which 4 samples (4%) violated the maximum residue limits. 4 samples violating the limit were all imported teas. Pesticides detected were chlorpyrifos, flufenoxuron, lufenuron, pyrimethanil and methoxyfenozide. These results indicate the need of continuous monitoring of pesticide residue needs for safety of flowering teas.

• Applied Biological Chemistry
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• v.32 no.1
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• pp.64-72
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• 1989

Near full length cDNA clones encoding the rice seed storage protein, prolamine, were isolated and divided into two homology classes based on cross-hybridization and DNA sequencing analysis. These cDNA clones contain a single open reading frame encoding a putative rice prolamine precursor(M.W.=17,200) possessing atypical 14 amino acid signal peptide. Clones of these two homology classes diverge mainly by insertions/deletions of short nucleotide stretches and point mutations. The deduced primary structures of both types of prolamine polypeptides are devoid of any major tandem repetitive sequences, a feature prevalent in other cereal prolamines. No significant homology teas detected between the rice prolamine and other cereal prolamines, indicating that the rice gene evolved from a different ancestor that gave rise to other cereal prolamine genes. Developing wheat and rice endosperms were examined using ultrathin sections prepared from tissues harvested at various days after flowering. By immunocytochemical localization techniques, wheat prolamines are localized within vesicles from Golgi apparatus and in homogeneous regions of protein bodies. The involvement of the goli apparatus in the packaging of wheat prolamines into protein bodies indicates a pathway which differs from the mode of other cereal prolamines and resembles the mechanism employed for the storage of rice glutelin and legume globulins.